The structure of deoxy and carbonmonoxy hemoglobin from Glycera debranchiatae and deoxy and cyan-met hemoglobin from the sea lamprey are being refined by a combination of real reciprocal space methods. The goal is to define as objectively as possible the structural changes that accompany the binding of ligands, i.e. to get a high resolution look at Perutz's "trigger." The computations are done via telephone line on Brookhaven's CDC 7600. Very poor diffraction patterns have been obtained from crystals of Earthworm hemoglobin (3x10 to the sixth power Daltons). Crystals of Limulus hemocyanin and of five of its subunits have been obtained. Two different forms of subunit #2 have unfavorably large lattices.